ID EFTU_PSEAB Reviewed; 397 AA. AC Q02T82; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 14-NOV-2006, sequence version 1. DT 27-MAR-2024, entry version 97. DE RecName: Full=Elongation factor Tu {ECO:0000255|HAMAP-Rule:MF_00118}; DE Short=EF-Tu {ECO:0000255|HAMAP-Rule:MF_00118}; GN Name=tuf1 {ECO:0000255|HAMAP-Rule:MF_00118}; Synonyms=tufB; GN OrderedLocusNames=PA14_08680; GN and GN Name=tuf2 {ECO:0000255|HAMAP-Rule:MF_00118}; Synonyms=tufA; GN OrderedLocusNames=PA14_08830; OS Pseudomonas aeruginosa (strain UCBPP-PA14). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=208963; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=UCBPP-PA14; RX PubMed=17038190; DOI=10.1186/gb-2006-7-10-r90; RA Lee D.G., Urbach J.M., Wu G., Liberati N.T., Feinbaum R.L., Miyata S., RA Diggins L.T., He J., Saucier M., Deziel E., Friedman L., Li L., Grills G., RA Montgomery K., Kucherlapati R., Rahme L.G., Ausubel F.M.; RT "Genomic analysis reveals that Pseudomonas aeruginosa virulence is RT combinatorial."; RL Genome Biol. 7:R90.1-R90.14(2006). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY, AND PHOSPHORYLATION AT TYR-77 AND RP TYR-88. RC STRAIN=UCBPP-PA14; RX PubMed=25096199; DOI=10.1007/s00216-014-8045-8; RA Ouidir T., Jarnier F., Cosette P., Jouenne T., Hardouin J.; RT "Potential of liquid-isoelectric-focusing protein fractionation to improve RT phosphoprotein characterization of Pseudomonas aeruginosa PA14."; RL Anal. Bioanal. Chem. 406:6297-6309(2014). CC -!- FUNCTION: This protein promotes the GTP-dependent binding of aminoacyl- CC tRNA to the A-site of ribosomes during protein biosynthesis. CC {ECO:0000255|HAMAP-Rule:MF_00118}. CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00118}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00118}. CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase CC superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00118}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP000438; ABJ13536.1; -; Genomic_DNA. DR EMBL; CP000438; ABJ13547.1; -; Genomic_DNA. DR RefSeq; WP_003115146.1; NZ_CP034244.1. DR AlphaFoldDB; Q02T82; -. DR SMR; Q02T82; -. DR iPTMnet; Q02T82; -. DR GeneID; 77219196; -. DR KEGG; pau:PA14_08680; -. DR KEGG; pau:PA14_08830; -. DR HOGENOM; CLU_007265_0_0_6; -. DR BioCyc; PAER208963:G1G74-721-MONOMER; -. DR BioCyc; PAER208963:G1G74-734-MONOMER; -. DR Proteomes; UP000000653; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule. DR GO; GO:0003924; F:GTPase activity; IEA:InterPro. DR GO; GO:0097216; F:guanosine tetraphosphate binding; IEA:UniProt. DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-UniRule. DR CDD; cd01884; EF_Tu; 1. DR CDD; cd03697; EFTU_II; 1. DR CDD; cd03707; EFTU_III; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR Gene3D; 2.40.30.10; Translation factors; 2. DR HAMAP; MF_00118_B; EF_Tu_B; 1. DR InterPro; IPR041709; EF-Tu_GTP-bd. DR InterPro; IPR004161; EFTu-like_2. DR InterPro; IPR033720; EFTU_2. DR InterPro; IPR031157; G_TR_CS. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR InterPro; IPR000795; T_Tr_GTP-bd_dom. DR InterPro; IPR009000; Transl_B-barrel_sf. DR InterPro; IPR009001; Transl_elong_EF1A/Init_IF2_C. DR InterPro; IPR004541; Transl_elong_EFTu/EF1A_bac/org. DR InterPro; IPR004160; Transl_elong_EFTu/EF1A_C. DR NCBIfam; TIGR00485; EF-Tu; 1. DR NCBIfam; TIGR00231; small_GTP; 1. DR PANTHER; PTHR43721:SF22; ELONGATION FACTOR TU, MITOCHONDRIAL; 1. DR PANTHER; PTHR43721; ELONGATION FACTOR TU-RELATED; 1. DR Pfam; PF00009; GTP_EFTU; 1. DR Pfam; PF03144; GTP_EFTU_D2; 1. DR Pfam; PF03143; GTP_EFTU_D3; 1. DR PRINTS; PR00315; ELONGATNFCT. DR SUPFAM; SSF50465; EF-Tu/eEF-1alpha/eIF2-gamma C-terminal domain; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR SUPFAM; SSF50447; Translation proteins; 1. DR PROSITE; PS00301; G_TR_1; 1. DR PROSITE; PS51722; G_TR_2; 1. PE 1: Evidence at protein level; KW Cytoplasm; Elongation factor; GTP-binding; Nucleotide-binding; KW Phosphoprotein; Protein biosynthesis. FT CHAIN 1..397 FT /note="Elongation factor Tu" FT /id="PRO_0000337471" FT DOMAIN 10..207 FT /note="tr-type G" FT REGION 19..26 FT /note="G1" FT /evidence="ECO:0000250" FT REGION 60..64 FT /note="G2" FT /evidence="ECO:0000250" FT REGION 81..84 FT /note="G3" FT /evidence="ECO:0000250" FT REGION 136..139 FT /note="G4" FT /evidence="ECO:0000250" FT REGION 174..176 FT /note="G5" FT /evidence="ECO:0000250" FT BINDING 19..26 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00118" FT BINDING 81..85 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00118" FT BINDING 136..139 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00118" FT MOD_RES 77 FT /note="Phosphotyrosine" FT /evidence="ECO:0000269|PubMed:25096199" FT MOD_RES 88 FT /note="Phosphotyrosine" FT /evidence="ECO:0000269|PubMed:25096199" SQ SEQUENCE 397 AA; 43370 MW; A019D5BF8EBAB942 CRC64; MAKEKFERNK PHVNVGTIGH VDHGKTTLTA ALTKVCSDTW GGSARAFDQI DNAPEEKARG ITINTSHVEY DSAVRHYAHV DCPGHADYVK NMITGAAQMD GAILVCSAAD GPMPQTREHI LLSRQVGVPY IVVFLNKADM VDDAELLELV EMEVRDLLNT YDFPGDDTPI IIGSALMALE GKDDNGIGVS AVQKLVETLD SYIPEPVRAI DQPFLMPIED VFSISGRGTV VTGRVERGII KVQEEVEIVG IKATTKTTCT GVEMFRKLLD EGRAGENVGI LLRGTKREDV ERGQVLAKPG TIKPHTKFEC EVYVLSKEEG GRHTPFFKGY RPQFYFRTTD VTGNCELPEG VEMVMPGDNI KMVVTLIAPI AMEDGLRFAI REGGRTVGAG VVAKIIE //